Information on EC 1.14.18.3 - methane monooxygenase (particulate)

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
1.14.18.3
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RECOMMENDED NAME
GeneOntology No.
methane monooxygenase (particulate)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
show the reaction diagram
methane + quinol + O2 = methanol + quinone + H2O
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Methane metabolism
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methane oxidation to methanol II
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SYSTEMATIC NAME
IUBMB Comments
methane,quinol:oxygen oxidoreductase
Contains copper. It is membrane-bound, in contrast to the soluble methane monooxygenase (EC 1.14.13.25).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Methylocystis sp.
strain Sc2
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain IMV 3011
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Manually annotated by BRENDA team
Soil bacterium
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-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,1,1-trifluoropropane + NAD(P)H + H+ + O2
(2R)-1,1,1-trifluoropropan-2-ol + (2S)-1,1,1-trifluoropropan-2-ol + NAD(P)+ + H2O
show the reaction diagram
-
-
the S stereoisomer is the dominant product
-
?
1,3-butadiene + duroquinol + O2
1,2-epoxybut-3-ene + duroquinone + H2O
show the reaction diagram
-
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100% 1,2-epoxybut-3-ene is produced, 36% (R)-selectivity, 64% (S)-selectivity
-
?
1-bromopropane + duroquinol + O2
1-bromo-2-propanol + 1-propanol + 1-bromo-3-propanol + duroquinone + H2O
show the reaction diagram
-
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72% 1-bromo-2-propanol (70% (R)-selectivity, 30% (S)-selectivity), 24% 1-propanol and 4% 1-bromo-3-propanol are produced
-
?
1-bromopropene + duroquinol + O2
1-bromo-2,3-epoxypropane + allyl-alcohol + 1-propanol + duroquinone + H2O
show the reaction diagram
-
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63% 1-bromo-2,3-epoxypropane, 31% allyl-alcohol and 6% 1-propanol are produced
-
?
1-butene + duroquinol + O2
1,2-epoxybutane + duroquinone + H2O
show the reaction diagram
-
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100% epoxybutane is produced, 36% (R)-selectivity, 64% (S)-selectivity
-
?
1-butene + NAD(P)H + H+ + O2
1,2-epoxybutane + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
1-butene + NAD(P)H + H+ + O2
3-buten-2-ol + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
1-chloropropane + duroquinol + O2
1-chloro-2-propanol + 1-propanol + 1-chloro-3-propanol + duroquinone + H2O
show the reaction diagram
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64% 1-chloro-2-propanol (70% (R)-selectivity, 30% (S)-selectivity), 29% 1-propanol and 7% 1-chloro-3-propanol are produced
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?
1-chloropropene + duroquinol + O2
1-chloro-2,3-epoxypropane + allyl-alcohol + 1-propanol + duroquinone + H2O
show the reaction diagram
-
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67% 1-chloro-2,3-epoxypropane, 23% allyl-alcohol and 10% 1-propanol are produced
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?
2-bromopropane + duroquinol + O2
2-bromo-1-propanol + acetone + duroquinone + H2O
show the reaction diagram
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2-bromo-1-propanol shows 26% (R)-selectivity and 74% (S)-selectivity
-
?
2-chloropropane + duroquinol + O2
2-chloro-1-propanol + ? + duroquinone + H2O
show the reaction diagram
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1-chloro-2-propanol shows 26% (R)-selectivity and 74% (S)-selectivity
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?
3,3,3-trifluoroprop-1-ene + NAD(P)H + H+ + O2
(2S)-2-(trifluoromethyl)oxirane + (2R)-2-(trifluoromethyl)oxirane + NAD(P)+ + H2O
show the reaction diagram
-
-
the S stereoisomer is the dominant product
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?
3,3,3-trifluoropropene + NAD(P)H + H+ + O2
?
show the reaction diagram
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-
-
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?
butane + duroquinol + O2
2-butanol + butanal + duroquinone + H2O
show the reaction diagram
-
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91% 2-butanal and 9% butanal are produced
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?
butane + NAD(P)H + H+ + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
show the reaction diagram
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?
cis-2-butene + duroquinol + O2
cis-2,3-epoxybutane + duroquinone + H2O
show the reaction diagram
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cis-2,3-epoxybutane is produced
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?
cis-2-butene + NAD(P)H + H+ + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
show the reaction diagram
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?
cis-but-2-ene + NAD(P)H + H+ + O2
cis-2,3-dimethyloxiran + NAD(P)+ + H2O
show the reaction diagram
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-
?
duroquinone + NAD(P)H + O2
duroquinol + NAD(P)+ + H2O
show the reaction diagram
ethane + duroquinol + O2
ethanal + duroquinone + H2O
show the reaction diagram
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100% ethanal is produced
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?
ethylene + duroquinol + O2
epoxyethane + duroquinone + H2O
show the reaction diagram
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100% epoxyethane produced
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?
formate + NAD(P)H + O2
?
show the reaction diagram
methane + duroquinol + O2
methanol + duroquinone + H2O
show the reaction diagram
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
methane + trans-dichloroethylene + vinyl chloride + trichloroethylene + O2
?
show the reaction diagram
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-
-
-
?
n-butane + NADH + O2
2-butanol + NAD+ + H2O
show the reaction diagram
n-pentane + NADH + O2
2-pentanol + NAD+ + H2O
show the reaction diagram
pentane + duroquinol + O2
2-pentanol + pentanal + duroquinone + H2O
show the reaction diagram
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31% 2-pentanal and 69% pentanal are produced
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?
pentane + NAD(P)H + H+ + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
show the reaction diagram
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?
propane + duroquinol + O2
2-propanol + propanal + duroquinone + H2O
show the reaction diagram
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84% 2-propanal and 16% propanal are produced
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?
propane + NAD(P)H + H+ + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
show the reaction diagram
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?
propene + NAD(P)H + H+ + O2
1,2-epoxypropane + NAD(P)+ + H2O
show the reaction diagram
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-
-
-
?
propene + NADH + H+ + O2
epoxypropane + NAD+ + H2O
show the reaction diagram
propene + NADH + H+ + O2
epoxypropene + NAD+ + H2O
show the reaction diagram
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57% (R)-selectivity, 43% (S)-selectivity
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?
propylene + 2,3-dimethylquinol + O2
propylene oxide + 2,3-dimethylquinone + H2O
show the reaction diagram
propylene + coenzyme Q0 + O2
propylene oxide + reduced coenzyme Q0 + H2O
show the reaction diagram
propylene + decyl-plastoquinol + O2
propylene oxide + decyl-plastoquinone + H2O
show the reaction diagram
propylene + decylubiquinol + O2
propylene oxide + decylubiquinone + H2O
show the reaction diagram
propylene + duroquinol + O2
epoxypropane + allyl-alcohol + 1-propanol + duroquinone + H2O
show the reaction diagram
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95% epoxypropane, 4.6% allyl-alcohol and 0.4% butanal are produced
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?
propylene + duroquinol + O2
propylene epoxide + duroquinone + H2O
show the reaction diagram
propylene + duroquinol + O2
propylene oxide + duroquinone + H2O
show the reaction diagram
propylene + duroquinol + O2
propylene oxide + reduced duroquinol + H2O
show the reaction diagram
propylene + menaquinol + O2
propylene oxide + menaquinone + H2O
show the reaction diagram
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-
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?
propylene + NAD(P)H + O2
propylene oxide + NADP+ + H2O
show the reaction diagram
propylene + NADH + H+ + O2
propylene oxide + NAD+ + H2O
show the reaction diagram
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
show the reaction diagram
propylene + NADH + O2
propylene oxide + NAD+ + H2O
show the reaction diagram
propylene + trimethylquinol + O2
propylene oxide + trimethylquinone + H2O
show the reaction diagram
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-
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?
trans-2-butene + duroquinol + O2
trans-2,3-epoxybutane + trans-2-butane-1-al + duroquinone + H2O
show the reaction diagram
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41% trans-2,3-epoxybutane and 59% trans-2-butane-1-al are produced
-
?
trans-2-butene + NAD(P)H + H+ + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
show the reaction diagram
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-
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-
?
trans-but-2-ene + NAD(P)H + H+ + O2
(2R,3R)-trans-2,3-dimethyloxirane + (2S,3S)-trans-2,3-dimethyloxirane + NAD(P)+ + H2O
show the reaction diagram
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the S,S stereoisomer is the dominant product
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
formate + NAD(P)H + O2
?
show the reaction diagram
methane + duroquinol + O2
methanol + duroquinone + H2O
show the reaction diagram
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
show the reaction diagram
methane + NADH + H+ + O2
methanol + NAD+ + H2O
show the reaction diagram
methane + NADH + O2
methanol + NAD+ + H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
succinate
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electron donor, membrane-bound enzyme
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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the enzyme contains three Co2+ ions per enzyme molecule
Fe
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pMMOH bears a binuclear iron valence site [Fe(III)-Fe(IV)]
Mn2+
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pMMO, low content
Mo2+
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pMMO, low content
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Heptyl-4-hydroxyquinoline-N-oxide
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pMMO, at 0.05 mM
Acetylene
copper
cyanide
duroquinol
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increasing duroquinol concentration above 70 mM causes almost total inhibition of enzyme activity
duroquinone
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noncompetitive inhibitor
EDTA
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18.1% residual activity at 1.5 mM
H2O2
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reversible inhibition of pMMO with H2O2 upon treatment of pMMO with H2O2 followed by the addition of catalase. H2O2 re-oxidizes the type 2 copper in pMMO reduced with duroquinol
Myxothiazol
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pMMO, suicide substrate
NaCl
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decrease in activity might be due to reduced enzyme solubility with increasing NaCl concentrations
propylene oxide
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product inhibition at higher concentration
additional information
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no detectable iron
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bacteriohemerythrin
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enhances enzyme activity. The maximum activity is observed at a enzyme to bacteriohemerythrin concentration ratio of 4:1
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catalase
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increases pMMO activity, catalyzes decomposition of H2O2, on pMMO activity
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Cu2+
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pMMO, optimal at 0.3 mM
Fe3+
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pMMO, optimal at 5.0 mM
lauryl maltoside
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the stimulatory effect of lauryl maltoside is responsible for the initial increase in duroquinol-dependent activity of the pellet, but no activity with NADH is observed after this solubilization
methanobactin-Cu2+ complex
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stimulation by methanobactin-Cu2+ complex, no activation in absence of copper, methanobactin is isolated from Methylosinus trichosporium strain OB3b
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additional information
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.003
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using propylene as substrate, pH and temperature not specified in the publication
0.0053
Methylocystis sp.
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using propylene as substrate, pH and temperature not specified in the publication
0.012
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purified enzyme, using propylene as substrate, in 25 mM MOPS buffer (pH 7.0), at 30C
0.016
using propylene as substrate, pH and temperature not specified in the publication
0.034
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purified enzyme, substrates propylene and duroquinol
0.0605
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whole cells, substrate formate
0.1037
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at 45C and pH 7.0, with NADH as cosubstrate, in the presence of bacteriohemerythrin
0.114
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membrane-bound enzyme, substrates propylene and duroquinol
0.1228
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at 45C and pH 7.0, with duroquinol as cosubstrate, in the presence of bacteriohemerythrin
0.16
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purified enzyme
0.23
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membrane-bound enzyme, substrates propylene and NADH
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.3
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
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apo-protein
200000
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non-denaturing PAGE
220000
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purified pMMO-detergent complex, gel filtration
390000
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gel filtration
660000
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solubilized enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotrimer
hexamer
oligomer
trimer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
heterotrimer of three subunits, pmoA, pmoB, and pmoC, with a solvent-exposed domain above the trans-membrane domain, which consists of alpha-helices
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to 2.8 A resolution
sitting drop vapor diffusion method, using 0.1 M MES, pH 6.5, 18% (w/v) PEG 750 MME, 0.03 M glycyl glycine, 0.01 M ZnSO4, at 22C
Methylocystis sp.
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hanging drop vapor diffusion method
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to 3.9 A resolution
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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or below: pMMO is irreversibly inactivated
438952
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
copper ions increase the stability of exfoliated pMMO
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instability of enzyme in crude extract
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pMMO is very unstable in vitro
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succinate stabilizes the membrane-bound enzyme
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to O2, 3 kinetically distinct froms of pMMO with respect to O2 tension, type I is stable with moderate activity, type II is highly unstable to oxygen, type III is an intermediate form
-
438952
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, pMMO is stable to proteolysis for many months
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-80C, pMMO kinetically type I with respect to O2-sensitivity, repeated freeze-thaw-cycles, stable
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4C, membrane-bound enzyme, activity is lost after 24 h, can be stabilized by succinate
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4C, pMMO in membrane fractions under nitrogen atmosphere, 4 days, 20% loss of activity
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4C, pMMO is stable to proteolysis for 1-2 weeks
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4C, reducing argon or nitrogen atmosphere, no loss of activity after 1 week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by centrifugation and gel filtration
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DEAE-Sepharose Fast Flow column chromatography, lysine agarose column chromatography, Sephacryl S-300HR gel filtration, QEA-Sephadex A-50 column chromatography, and Sephacryl S200 gel filtration, Superdex 200 gel filtration, or ammonium sulfate precipitation followed by Source 30Q column chroamtography
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FPLC liquid chromatography and Mono Q HR 5/50 GL column chromatography
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membrane-associated methane-oxidizing complex consisting of the particulate methane mono-oxygenase, pMMOH, and an unidentified component, assigned as a potential particulate methane mono-oxygenase reductase, pMMOR
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MonoQ 10/100 GL column chromatography and Sephacryl S100 gel filtration
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Ni2+-Sepharose Fast Flow column chromatography
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optimization of solubilization and purification procedure for the hydroxylase component of membrane-bound enzyme, purification to homogeneity involves solubilization by dodexylbeta-D-maltoside, ion exchange chromatography and gel filtration, the purification includes the loss of the reductase component
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partially by preparation of washed membranes
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particulate form of methane hydroxylase (pMH) obtained by ion exchange and hydrophobic chromatography
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pMMO after induction with copper, kinetic type I with respect to O2-sensitivity
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POROS 20HQ column chromatography, gel filtration. Purified pMMO is inherently instable in vitro
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stable and active native pMMO from membranes, by solubilization with 1% w/v CHAPS, removal of soluble proteins, gel filtration, anion exchange chromatography, and ultrafiltration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and anaylsis, the gene is organized in the structural gene cluster pmoCAB, stable functional expression of the membrane-bound enzyme in Rhodococcus erythropolis strain LSSE8-1 by using the dsz promoter and ethane as the sole carbon source, method optimization, overview
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expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21(DE3) or Rosetta (DE3) pLysS cells
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genetic analysis of pMMO genes
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pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells; pmoA cloned in pGEM-T Easy vector and transformed into Escherichia coli JM109 high-efficiency competent cells
two aqueous-exposed subdomains toward the N- and C-termini of the large subunit are expressed in Escherichia coli BL21 (DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a 10fold downregulation of the pmoA2 gene is observed when Methylacidiphilum kamchatkense strain Kam1 is grown on methanol as carbon and energy source. The expression of the other three pmoA genes is also affected by the substrate switch from methane to methanol, but to a lesser extent than pmoA2
for pMMO-expressing conditions, 0.02 mM copper is added and is equilibrated for at least 1 day before the media are inoculated
-
pMMO is expressed at high copper/biomass ratios
pMMO is produced when the copper/biomass ratio is high
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the pMMO enzyme is expressed in cells grown under high copper-to-biomass ratios
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H137A/H139A
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the mutant of subunit domain spmoB disrupts the dicopper site and exhibits no activity
H48N
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the mutant of subunit domain spmoB disrupts the monocopper site, but still exhibits enzyme activity
H48N/H137A/H139A
-
the mutant of subunit domain spmoB disrupts the dicopper site and exhibits no activity
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
copper ions increase the stability of exfoliated pMMO
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
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pMMO can be used for biodegradation of mixtures of chlorinated solvents, i.e., trichloroethylene, trans-dichloroethylene, and vinyl chloride. If the concentrations are increased to 0.1 mM, pMMO-expressing cells grow faster and degrade more of these pollutants in a shorter amount of time than sMMO
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